PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 6324327

From Virchow to red cells (the unended quest).

G A Marcel·C George·D Weill·E Catry·M Thao-Chan
View original source ↗Export metadata ↓

Abstract

For Virchow vessel wall, coagulability and flow were the three eventual culprits of thrombogenesis. Pharmacological progress in the three fields has not been parallel. Strangely enough they have found possible therapy in the order of their description: first the vessel wall with vasodilators. Then 'coagulability' with anticoagulants, thrombolytics, antiaggregants. It is only more recently that new methods of investigation have allowed assessment and pharmacology of the main determinant of flow in microvessels: red cell deformability.

Explore related subjects

2,3-DiphosphoglycerateAnimalsBloodBlood ViscosityCalciumCardiovascular DiseasesCyclic AMPDiphosphoglyceric AcidsErythrocytesFibrinolysisHumansModels, BiologicalPlatelet AggregationThrombosisUltrafiltrationVasodilationJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

G A Marcel, C George, D Weill, E Catry, M Thao-Chan. 1983. From Virchow to red cells (the unended quest).. https://pubmed.ncbi.nlm.nih.gov/6324327/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2006

Erythrocyte oxidative damage in chronic fatigue syndrome.

BACKGROUND: It has been hypothesized that a link exists between erythrocyte metabolism (particularly redox metabolism) and erythrocyte shape and that both are related to erythrocyte deformability. The aim of this research is to confirm the results of earlier studies and to investigate a correlation between erythrocyte morphology and erythrocyte oxidative damage in chronic fatigue syndrome (CFS). METHODS: Reduced glutathione (GSH), malondialdehyde (MDA), methemoglobin (metHb) and 2,3-diphosphoglyceric acid (2,3-DPG) were measured in 31 patients suffering from CFS and 41 healthy control subjects. Scanning electron microscopic studies of the erythrocytes from both groups were also carried out. RESULTS: There was evidence of oxidative damage in CFS with statistically significant increases in 2,3-DPG (p < 0.05), metHb (p < 0.005) and MDA (p < 0.01). The CFS patients in this study also had significantly more stomatocytes in their blood than the normal subjects (p < 0.005). CONCLUSIONS: There is a strong likelihood that the increase in erythrocyte antioxidant activity is associated with the presence of stomatocytes. The results of this study provide further evidence for the role of free radicals in the pathogenesis of CFS and a link between erythrocyte metabolism and erythrocyte shape.

2,3-Diphosphoglycerate↗
PubMed2006

Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.

Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin. In this paper, we directly observed real-time motion of the enzyme active site and the substrate during phosphoryl transfer. A series of high resolution crystal structures of human bisphosphoglycerate mutase co-crystallized with 2,3-bisphosphoglycerate, representing different time points in the phosphoryl transfer reaction, were solved. These structures not only clarify the argument concerning the substrate binding mode for this enzyme family but also depict the entire process of the key histidine phosphorylation as a "slow movie". It was observed that the enzyme conformation continuously changed during the different states of the reaction. These results provide direct evidence for an "in line" phosphoryl transfer mechanism, and the roles of some key residues in the phosphoryl transfer process are identified.

2,3-Diphosphoglycerate↗
PubMed2006

Analysis of oxygen binding by hemoglobin on the basis of mean intrinsic thermodynamic quantities.

The binding data for oxygenation of human hemoglobin, Hb, at various temperatures and in the absence and presence of 2,3-diphosphoglycerate, DPG, and inositol hexakis phosphate, IHP, were analyzed for extraction of mean intrinsic Gibbs free energy, DeltaGo, enthalpy, DeltaHo, and entropy, DeltaSo, of binding at various partial oxygen pressures. This method of analysis considers all the protein species present such as dimer and tetramer forms which were not considered by Imai et al. (Imai K et al., 1970, Biochim Biophys Acta 200: 189-196), in their analysis which was based on Adair equation. In this regard, the values of Hill equation parameters were estimated with high precision at all points of the binding curve and used for calculation of DeltaGo, DeltaHo and DeltaSo were also calculated by analysis of DeltaGo values at various temperatures using van't Hoff equation. The results represent the enthalpic nature of the cooperativity in Hb oxygenation and the compensation effect of intrinsic entropy. The interpretation of results also to be, into account the decrease of the binding affinity of sites for oxygen in the presence of DPG and IHP without any considerable changes in the site-site interaction (extent of cooperativity). In other words, the interactions between bound ligands, organic phosphates and oxygen, are more due to a decreasing binding affinity and not to the reduction of the cooperative interaction between sites. The results also document the more heterotropic effect of IHP compared to DPG.

2,3-Diphosphoglycerate↗